O95147 (DUS14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 14
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
MKP-1-like protein tyrosine phosphatase
Short name=MKP-L
Mitogen-activated protein kinase phosphatase 6
Short name=MAP kinase phosphatase 6
Short name=MKP-6

Gene names

Name:	DUSP14
Synonyms:	MKP6

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Interacts with CD28.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 198

198

Dual specificity protein phosphatase 14

PRO_0000094822

Regions

Domain

91 – 156

66

Tyrosine-protein phosphatase

Sites

Active site

111

1

Phosphocysteine intermediate Ref.5

Amino acid modifications

Modified residue

7

1

Phosphoserine Ref.4

Modified residue

8

1

Phosphothreonine Ref.4

Secondary structure

1

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198

Helix Strand Turn

Details...

Beta strand

28 – 31

4

Beta strand

34 – 36

3

Helix

45 – 50

6

Beta strand

55 – 58

4

Beta strand

61 – 63

3

Beta strand

71 – 75

5

Helix

90 – 102

13

Beta strand

107 – 110

4

Helix

117 – 130

14

Helix

134 – 144

11

Helix

155 – 165

11

Helix

183 – 189

7

Sequences

	Sequence		Length	Mass (Da)
	O95147 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 6AAFAE1B3A24F9AA	FASTA	198	22,255
	10 20 30 40 50 60 MSSRGHSTLP RTLMAPRMIS EGDIGGIAQI TSSLFLGRGS VASNRHLLQA RGITCIVNAT 70 80 90 100 110 120 IEIPNFNWPQ FEYVKVPLAD MPHAPIGLYF DTVADKIHSV SRKHGATLVH CAAGVSRSAT 130 140 150 160 170 180 LCIAYLMKFH NVCLLEAYNW VKARRPVIRP NVGFWRQLID YERQLFGKST VKMVQTPYGI 190 VPDVYEKESR HLMPYWGI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MKP-L, a novel MKP-1 like protein tyrosine phosphatase." Yuan Y., Suphapeetiporn K., Sun H. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Negative-feedback regulation of CD28 costimulation by a novel mitogen-activated protein kinase phosphatase, MKP6." Marti F., Krause A., Post N.H., Lyddane C., Dupont B., Sadelain M., King P.D. J. Immunol. 166:197-206(2001) [PubMed: 11123293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[4]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND THR-8, MASS SPECTROMETRY.
[5]	"Overproduction, purification and structure determination of human dual-specificity phosphatase 14." Lountos G.T., Tropea J.E., Cherry S., Waugh D.S. Acta Crystallogr. D 65:1013-1020(2009) [PubMed: 19770498] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 2-191 IN COMPLEX WITH PHOSPHATE, ACTIVE SITE, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF038844 mRNA. Translation: AAD02105.1.
AF120032 mRNA. Translation: AAF28861.1.
BC000370 mRNA. Translation: AAH00370.1.
BC001894 mRNA. Translation: AAH01894.1.
BC004448 mRNA. Translation: AAH04448.1.

IPI

IPI00013031.

RefSeq

NP_008957.1. NM_007026.2.

UniGene

Hs.91448.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WGP	X-ray	1.88	A/B	2-191	[»]

ProteinModelPortal

O95147.

SMR

O95147. Positions 24-191.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95147. 1 interaction.

STRING

O95147.

PTM databases

PhosphoSite

O95147.

Proteomic databases

PeptideAtlas

O95147.

PRIDE

O95147.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000292964; ENSP00000292964; ENSG00000161326.
ENST00000394386; ENSP00000377910; ENSG00000161326.
ENST00000394389; ENSP00000377912; ENSG00000161326.

GeneID

11072.

KEGG

hsa:11072.

UCSC

uc002hnx.2. human.

Organism-specific databases

CTD

11072.

GeneCards

GC17P035850.

H-InvDB

HIX0013746.

HGNC

HGNC:17007. DUSP14.

HPA

HPA019911.

MIM

606618. gene.

neXtProt

NX_O95147.

PharmGKB

PA27523.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15835.

HOGENOM

HBG717377.

HOVERGEN

HBG051422.

InParanoid

O95147.

OMA

YLMKCHS.

OrthoDB

EOG48PMM7.

PhylomeDB

O95147.

Gene expression databases

ArrayExpress

O95147.

Bgee

O95147.

CleanEx

HS_DUSP14.

Genevestigator

O95147.

GermOnline

ENSG00000161326. Homo sapiens.

Family and domain databases

InterPro

IPR020417. Dual-sp_phosphatase.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020420. Dual-sp_phosphatase_famB.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR000387. Tyr/Dual-specificity_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]

KO

K04459.

Pfam

PF00782. DSPc. 1 hit.
[Graphical view]

PRINTS

PR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.

SMART

SM00195. DSPc. 1 hit.
[Graphical view]

PROSITE

PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

42090.

SOURCE

Search...

Entry information

Entry name

DUS14_HUMAN

Accession

Primary (citable) accession number: O95147

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.